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Journal of Bacteriology, September 1999, p. 5557-5562, Vol. 181, No. 18
Department of Life Sciences and Chemistry,
Received 26 March 1999/Accepted 2 July 1999
Expression of the dnaA gene continues in the lag phase
following a temperature downshift, indicating that DnaA is a cold shock protein. Steady-state DnaA protein concentration increases at low
temperatures, being twofold higher at 14°C than at 37°C. DnaA protein was found to be stable at both low and high temperatures. Despite the higher DnaA concentration at low temperatures, the mass per
origin, which is proportional to the initiation mass, was the same at
all temperatures. Cell size and cellular DNA content decreased
moderately below 30°C due to a decrease in the time from termination
to division relative to generation time at the lower temperatures.
Analysis of dnaA gene expression and initiation of
chromosome replication in temperature shifts suggests that a fraction
of newly synthesized DnaA protein at low temperatures is irreversibly
inactive for initiation and for autorepression or that all DnaA protein
synthesized at low temperatures has an irreversible low-activity conformation.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Low-Temperature-Induced DnaA Protein Synthesis Does
Not Change Initiation Mass in Escherichia coli
K-12
*
Corresponding author. Mailing address: Department of
Life Sciences and Chemistry, Roskilde University, DK-4000 Roskilde,
Denmark. Phone: (45) 46 74 24 02. Fax: (45) 46 74 30 11. E-mail:
atlung{at}ruc.dk.
Journal of Bacteriology, September 1999, p. 5557-5562, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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